Lysozyme enhances monocyte-mediated tumoricidal activity

A potential amplifying mechanism of tumor killing

P. LeMarbre, J. J. Rinehart, Neil Elliot Kay, R. Vesella, H. S. Jacob

Research output: Contribution to journalArticle

35 Citations (Scopus)

Abstract

The mononuclear phagocyte is well established as an in vitro cytotoxic effector cell for certain human tumors. The mechanism(s) for this action remains unclear. Increased levels of lysozyme, a cationic enzyme synthesized in large amounts by mononuclear phagocytes, are associated with increased resistance to transplantable animal tumors. In this study, we provide evidence that human lysozyme, isolated from the urine of leukemic patients, has marked potentiating effects on human monocyte-tumor-cell cytocidal activity. In addition, lysozyme-exposed monocytes incorporate increased quantities of leucine, suggesting that monocytes are capable of amplifying their own metabolic activation by secreting an endogenous constituent. Tri-N-acetyl-glucosamine, a competitive inhibitor for the active site of lysozyme, inhibits cytocidal activity. Conversely, protamine, an extraneous albeit similarly positively charged molecule, increases monocyte-mediated tumor cytotoxicity; this protamine effect is negated by heparin. We conclude that lysozyme, at least partially by its positive charge, is capable of enhancing in vitro monocyte tumor cell cytotoxicity; its in vivo secretion may potentiate monocyte-tumor-cell interaction.

Original languageEnglish (US)
Pages (from-to)994-999
Number of pages6
JournalBlood
Volume58
Issue number5
StatePublished - 1981
Externally publishedYes

Fingerprint

Muramidase
Tumors
Monocytes
Neoplasms
Protamines
Cytotoxicity
Phagocytes
Glucosamine
Leucine
Cell Communication
Heparin
Catalytic Domain
Animals
Chemical activation
Cells
Urine
Molecules
Enzymes

ASJC Scopus subject areas

  • Hematology

Cite this

LeMarbre, P., Rinehart, J. J., Kay, N. E., Vesella, R., & Jacob, H. S. (1981). Lysozyme enhances monocyte-mediated tumoricidal activity: A potential amplifying mechanism of tumor killing. Blood, 58(5), 994-999.

Lysozyme enhances monocyte-mediated tumoricidal activity : A potential amplifying mechanism of tumor killing. / LeMarbre, P.; Rinehart, J. J.; Kay, Neil Elliot; Vesella, R.; Jacob, H. S.

In: Blood, Vol. 58, No. 5, 1981, p. 994-999.

Research output: Contribution to journalArticle

LeMarbre, P, Rinehart, JJ, Kay, NE, Vesella, R & Jacob, HS 1981, 'Lysozyme enhances monocyte-mediated tumoricidal activity: A potential amplifying mechanism of tumor killing', Blood, vol. 58, no. 5, pp. 994-999.
LeMarbre, P. ; Rinehart, J. J. ; Kay, Neil Elliot ; Vesella, R. ; Jacob, H. S. / Lysozyme enhances monocyte-mediated tumoricidal activity : A potential amplifying mechanism of tumor killing. In: Blood. 1981 ; Vol. 58, No. 5. pp. 994-999.
@article{3303080bfe394e168fdbe57bae1b70bf,
title = "Lysozyme enhances monocyte-mediated tumoricidal activity: A potential amplifying mechanism of tumor killing",
abstract = "The mononuclear phagocyte is well established as an in vitro cytotoxic effector cell for certain human tumors. The mechanism(s) for this action remains unclear. Increased levels of lysozyme, a cationic enzyme synthesized in large amounts by mononuclear phagocytes, are associated with increased resistance to transplantable animal tumors. In this study, we provide evidence that human lysozyme, isolated from the urine of leukemic patients, has marked potentiating effects on human monocyte-tumor-cell cytocidal activity. In addition, lysozyme-exposed monocytes incorporate increased quantities of leucine, suggesting that monocytes are capable of amplifying their own metabolic activation by secreting an endogenous constituent. Tri-N-acetyl-glucosamine, a competitive inhibitor for the active site of lysozyme, inhibits cytocidal activity. Conversely, protamine, an extraneous albeit similarly positively charged molecule, increases monocyte-mediated tumor cytotoxicity; this protamine effect is negated by heparin. We conclude that lysozyme, at least partially by its positive charge, is capable of enhancing in vitro monocyte tumor cell cytotoxicity; its in vivo secretion may potentiate monocyte-tumor-cell interaction.",
author = "P. LeMarbre and Rinehart, {J. J.} and Kay, {Neil Elliot} and R. Vesella and Jacob, {H. S.}",
year = "1981",
language = "English (US)",
volume = "58",
pages = "994--999",
journal = "Blood",
issn = "0006-4971",
publisher = "American Society of Hematology",
number = "5",

}

TY - JOUR

T1 - Lysozyme enhances monocyte-mediated tumoricidal activity

T2 - A potential amplifying mechanism of tumor killing

AU - LeMarbre, P.

AU - Rinehart, J. J.

AU - Kay, Neil Elliot

AU - Vesella, R.

AU - Jacob, H. S.

PY - 1981

Y1 - 1981

N2 - The mononuclear phagocyte is well established as an in vitro cytotoxic effector cell for certain human tumors. The mechanism(s) for this action remains unclear. Increased levels of lysozyme, a cationic enzyme synthesized in large amounts by mononuclear phagocytes, are associated with increased resistance to transplantable animal tumors. In this study, we provide evidence that human lysozyme, isolated from the urine of leukemic patients, has marked potentiating effects on human monocyte-tumor-cell cytocidal activity. In addition, lysozyme-exposed monocytes incorporate increased quantities of leucine, suggesting that monocytes are capable of amplifying their own metabolic activation by secreting an endogenous constituent. Tri-N-acetyl-glucosamine, a competitive inhibitor for the active site of lysozyme, inhibits cytocidal activity. Conversely, protamine, an extraneous albeit similarly positively charged molecule, increases monocyte-mediated tumor cytotoxicity; this protamine effect is negated by heparin. We conclude that lysozyme, at least partially by its positive charge, is capable of enhancing in vitro monocyte tumor cell cytotoxicity; its in vivo secretion may potentiate monocyte-tumor-cell interaction.

AB - The mononuclear phagocyte is well established as an in vitro cytotoxic effector cell for certain human tumors. The mechanism(s) for this action remains unclear. Increased levels of lysozyme, a cationic enzyme synthesized in large amounts by mononuclear phagocytes, are associated with increased resistance to transplantable animal tumors. In this study, we provide evidence that human lysozyme, isolated from the urine of leukemic patients, has marked potentiating effects on human monocyte-tumor-cell cytocidal activity. In addition, lysozyme-exposed monocytes incorporate increased quantities of leucine, suggesting that monocytes are capable of amplifying their own metabolic activation by secreting an endogenous constituent. Tri-N-acetyl-glucosamine, a competitive inhibitor for the active site of lysozyme, inhibits cytocidal activity. Conversely, protamine, an extraneous albeit similarly positively charged molecule, increases monocyte-mediated tumor cytotoxicity; this protamine effect is negated by heparin. We conclude that lysozyme, at least partially by its positive charge, is capable of enhancing in vitro monocyte tumor cell cytotoxicity; its in vivo secretion may potentiate monocyte-tumor-cell interaction.

UR - http://www.scopus.com/inward/record.url?scp=0019842272&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0019842272&partnerID=8YFLogxK

M3 - Article

VL - 58

SP - 994

EP - 999

JO - Blood

JF - Blood

SN - 0006-4971

IS - 5

ER -